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Effects of cytochalasin congeners, microtubule-directed agents, and doxorubicin alone or in combination against human ovarian carcinoma cell lines in vitro

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Although the actin cytoskeleton is vital for carcinogenesis and subsequent pathology, no microfilament-directed agent has been approved for cancer chemotherapy. One of the most studied classes of microfilament-directed agents has been the cytochalasins, mycotoxins known to disrupt the formation of actin polymers.

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R E S E A R C H A R T I C L E Open Access

Effects of cytochalasin congeners,

microtubule-directed agents, and doxorubicin

alone or in combination against human

ovarian carcinoma cell lines in vitro

Matthew Trendowski*, Timothy D Christen, Christopher Acquafondata and Thomas P Fondy

Abstract

Background: Although the actin cytoskeleton is vital for carcinogenesis and subsequent pathology, no

microfilament-directed agent has been approved for cancer chemotherapy One of the most studied classes of microfilament-directed agents has been the cytochalasins, mycotoxins known to disrupt the formation of actin polymers In the present study, we sought to determine the effects of cytochalasin congeners toward human drug sensitive and multidrug resistant cell lines

Methods: SKOV3 human ovarian carcinoma and several multidrug resistant derivatives were tested for sensitivity against a panel of nine cytochalasin congeners, as well as three clinically approved chemotherapeutic agents (doxorubicin, paclitaxel, and vinblastine) In addition, verapamil, a calcium ion channel blocker known to reverse P-glycoprotein (P-gp) mediated drug resistance, was used in combination with multiple cytochalasin congeners to determine whether drug sensitivity could be increased

Results: While multidrug resistant SKVLB1 had increased drug tolerance (was more resistant) to most cytochalasin congeners in comparison to drug sensitive SKOV3, the level of resistance was 10 to 1000-fold less for the cytochalasins than for any of the clinically approved agents While cytochalasins did not appear to alter the expression of ATP binding cassette (ABC) transporters, several cytochalasins appeared to inhibit the activity of ABC transporter-mediated efflux of rhodamine 123 (Rh123), suggesting that these congeners do have affinity for drug efflux pumps Cytochalasins also appeared to significantly decrease the F/G-actin ratio in both drug sensitive and drug resistant cells, indicative of marked microfilament inhibition The cytotoxicity of most cytochalasin congeners could be increased with the addition

of verapamil, and the drug sensitivity of resistant SKVLB1 to the clinically approved antineoplastic agents could be increased with the addition of cytochalasins As assessed by isobolographic analysis and Chou-Talalay statistics,

cytochalasin B and 21,22-dihydrocytochalasin B (DiHCB) demonstrated notable synergy with doxorubicin and

paclitaxel, warranting further investigation in a tumor-bearing mammalian model

Conclusion: Cytochalasins appear to inhibit the activity of P-gp and potentially other ABC transporters, and may have novel activity against multidrug resistant neoplastic cells that overexpress drug efflux proteins

* Correspondence: mrtrendo@syr.edu

Department of Biology, Syracuse University, 107 College Place, Syracuse, NY

13244, USA

© 2015 Trendowski et al Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made The Creative Commons Public Domain Dedication waiver

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Cytochalasins are mycotoxins known to disrupt the

for-mation of filamentous (F)-actin, thereby preventing the

formation of functional microfilaments These congeners

are characterized by a highly substituted

perhydro-isoindolone structure that is typically attached to a

macro-cyclic ring [1] More than 60 different cytochalasins from

several species of fungi have been classified into various

subgroups based on the size of the macrocyclic ring and

the substituent of the perhydroisoindolyl-1-one residue at

the C-3 position [2]; structures of representative

cytocha-lasins are shown in Fig 1 While most of our previous

work has focused on cytochalasin B, there are many other

congeners with similar activity toward microfilaments As

microfilament-disrupting agents, cytochalasins alter cell

motility, adherence, secretion, drug efflux, deformability,

morphology, and size, among many other cell properties

critical to neoplastic cell pathology [1, 2] In addition, two

of the congeners (cytochalasins B and D) have shown

par-tial specificity against neoplastic cells [3–10], consistent

with the substantial differences known to exist between

the microfilament biochemistry of neoplastic and normal

cells [11, 12] These differences in microfilament structure

may be related to key neoplastic characteristics, including

altered adherence, anchorage independent growth,

inva-siveness, and altered plasma membrane cytoskeletal

inter-actions involving expression of oncoproteins [12, 13]

Previously, we have demonstrated that cytochalasin B and its reduced congener 21,22-dihydrocytochalasin B (DiHCB) are able to sensitize multidrug resistant P388/ ADR murine leukemia cells to doxorubicin, with both con-geners showing considerable drug synergy with the nucleic acid-directed agent [14] In addition, prior research has indicated that cytochalasin B efflux is less affected by over-expression of ATP binding cassette (ABC) transporters than other cytotoxic drug classes (vinca alkaloids and anthracyclines) [15] that often exhibit drug resistance in the clinical setting Based on these observations, it appears that cytochalasin B and potentially other cytochalasin congeners might be active against multidrug resistant neoplastic cells and might also be able to overcome resistance to other cytotoxic agents currently used in the clinical setting Therefore, this study seeks to determine the effects of cyto-chalasin congeners toward drug sensitive and multidrug resistant human cancer cell lines

SKOV3 is a human ovarian carcinoma cell line frequently used in vitro and also in vivo as a xenograft in immunosup-pressed mice SKOV3 cells have slight, but noticeable resist-ance to tumor necrosis factor, as well as to cisplatin and doxorubicin [16, 17] The inherent drug resistance of SKOV3 cells can be dramatically elevated through progres-sively increasing exposure to either vinblastine or vincris-tine [18] One of the most notable multidrug resistant cell lines, SKVLB1, is 2,000-fold more resistant to vinblastine,

Fig 1 Molecular structure of the cytochalasin macrocycle and several congeners The macrocycle skeleton of cytochalasins is provided to indicate the numbering system used for these congeners In addition, the structure of 21,22-dihydrocytochalasin B is shown to indicate the differences in structure it has with the γ-lactone derivative The α, β-unsaturated ketones of cytochalasin A runs from C-20 to C-23

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10,000-fold more resistant to vincristine, 260-fold more

resistant to doxorubicin, and 510-fold more resistant to

the non-clinically approved colchicine when compared to

the parental cell line [18] Further, this increase in drug

resistance is mirrored by increasing overexpression of

P-glycoprotein (P-gp), a known ABC transporter [19, 20]

Since cytochalasin B efflux is notably resistant to P-gp

overexpression, drug sensitive and drug resistant SK

human ovarian carcinoma cell lines are ideal models to

examine cytochalasin sensitivity in multidrug resistant

cancers These cell lines can also reveal potential drug

synergism when cytochalasin congeners are combined

with chemotherapeutic agents, or with calcium ion

chan-nel blockers known to inhibit P-gp drug efflux [20–24]

Methods

Preparation of human ovarian carcinoma cell lines

SK human ovarian carcinoma cell lines with varying levels

of drug resistance were provided courtesy of Dr Victor

Ling (University of British Columbia, Canada) The level

of drug resistance of the cell lines from lowest to highest

is as follows: SKOV3 (parental cell line), SKVCR0.015,

SKVCR0.1, and SKVLB1 (see Reference [18] for details on

how drug resistance is acquired) All cell lines were seeded

sus-pended in 9 ml of RPMI 1640 complete medium

contain-ing 10 % newborn calf serum (GIBCO, Grand Island, NY,

37 °C During subculture, cells were trypsinized with

0.05 % trypsin-EDTA solution 1X (Sigma-Aldrich Corp., St

Louis, MO, USA) for 5 min at 37 °C, dislodged by a sharp

knocking of the flasks during that period, washed, diluted

were seeded into 25 cm2culture flasks (4 × 104cells/cm2)

Cytochalasin B preparation

Cytochalasin B was prepared from mold mattes of

described [13, 14, 25], and purified by preparative thin

layer chromatography to greater than 99 % homogeneity

after recrystallization from chloroform Cytochalasin B

and other cytochalasins prepared in our laboratory were

shown), and were compared to commercially acquired

samples (Sigma-Aldrich Corp.) to ensure that the

iso-lated products were of a suitable grade

21, 22-Dihydrocytochalasin B Preparation

DiHCB was prepared by sodium borohydride reduction of

cytochalasin B in methanol at 25 °C as previously described

[14, 26] The product was recovered as a

chloroform-soluble fraction and crystallized from benzene:hexane

DiHCB was compared to a commercially purchased

sample of DiHCB (Sigma-Aldrich Corp.) and cytocha-lasin B (Sigma-Aldrich Corp.) using reverse phase thin layer chromatography

Cytochalasin D preparation Cytochalasin D was prepared from mold mattes of

described [14, 26], and purified by preparative thin layer chromatography to greater than 99 % homogen-eity after recrystallization from chloroform

Cytochalasin C preparation Cytochalasin C was prepared through an isomerization reaction of cytochalasin D using a Pd/charcoal catalyst at

25 °C as previously described [26] After filtration of the charcoal catalyst, cytochalasin C was isolated from any remaining cytochalasin D in the reaction product using

C-18 reverse phase thin layer chromatography plates with methanol:water, 75:25 v/v as mobile phase, followed by fluorescence quenching A small amount of commercial cytochalasin C (Sigma-Aldrich Corp.) was characterized

by reverse phase thin layer chromatography and recrystal-lized from acetone:hexane for comparison with the puri-fied product

Preparation of other cytochalasin congeners All other cytochalasin congeners (cytochalasins A, E, H,

J, and DiHCBγ-L), were acquired commercially (Sigma-Aldrich Corp.) All cytochalasins used in the study were

EtOH in conical 1.5 ml plastic centrifuge tubes Once the

10 mg/ml cytochalasin/EtOH solution was diluted into

EtOH

Preparation of clinically approved chemotherapeutic agents

Doxorubicin, paclitaxel, and vinblastine were acquired commercially (Sigma-Aldrich Corp.) Doxorubicin was solubilized in isotonic saline, paclitaxel in 1:1 100 % EtOH: Kolliphor EL, and vinblastine in sterilized water Plate assay procedures

SK human ovarian carcinoma cells were tested for drug sensitivity using 24-well assay plates (Corning Life Sci-ences, Corning, NY, USA) Each well contained ~ 1000 cells in 1 ml medium Agents were then dissolved in the wells at varying concentrations for 23 wells, while the last well remained untreated The plates were incubated at

37 °C for the length of drug exposure, and then stained with methylene blue This method was then used to assess varying inhibitory concentrations of each agent alone or in combination with another agent as described in [18] The

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efficacy of the method was also confirmed with a XTT

cells were seeded per well into a flat-bottom 96-well

microtiter plate in triplicate for each cell dilution The

plate was incubated for 24 h prior to addition of XTT

solution Cells were then incubated for an additional 2 h

before the wavelength was read

Examining the effects of cytochalasins on microfilaments

in neoplastic cells

Cytochalasins were assessed for their ability to inhibit the

formation of F-actin by examining the ratio of F-actin to

monomeric globular (G)-actin found within the SK human

ovarian cancer cell lines prior to and after treatment The

F-actin to G-actin ratio was determined with the G-Actin/

F-Actin In Vivo Assay Biochem Kit (Cytoskeleton Inc.,

Denver, CO, USA) After being treated, cells were lysed

with LAS2 buffer (1 ml lysis and F-actin stabilization buffer,

100× protease inhibitor cocktail stock solution) on ice for

10 min Cells were collected and the cell extracts were

centrifuged at 4 °C for 75 min at 16,000 g to separate the

F-actin and G-F-actin pools The supernatants of the extracts

were collected and designated as the G-actin pool The

pellets were resuspended in ice-cold actin depolymerization

buffer and designated as the F-actin pool Equal amounts of

both the supernatant (G-actin) and the resuspended pellet

(F-actin) were subjected to Western blot analysis with the

use of an anti-β-actin antibody

Assessing the inhibitory activity cytochalasins have

toward ATP binding cassette transporters

To determine whether cytochalasins exert antineoplastic

activity via inhibition of P-gp and other ABC transporters,

reverse transcription polymerase chain reaction (RT-PCR)

was used to quantify the RNA levels of three ABC

trans-porters; P-gp (ABCB1), Multidrug resistance-associated

protein 1 (MRP1; ABCC1) and multidrug

resistance-associated protein 2 (MRP2; ABCC2) Total RNA was

extracted from cells according to instructions provided in

the RNeasy Mini kit (Qiagen Inc., Valencia, CA, USA)

Suc-cessfully extracted RNA was then dissolved in

diethylpyro-carbonate/water Absorption values were read at 260 nm

and 280 nm using a UV spectrophotometer Acquired RNA

was converted into cDNA according to the instructions

provided in the RT-PCR kit (Life Technologies, Grand

Island, NY, USA), and primers used for RT-PCR are shown

in Table 1 The reaction was carried out under the

follow-ing conditions: denaturation at 95 °C for 5 min with an

additional 15 s at 94 °C, and a 30 s annealing at 60 °C

Targets genes were directly quantified to the reference gene

β-actin, since cytochalasins do not significantly affect the

RNA expression levels of actin [1]

In addition to examining the effects of cytochalasins on the RNA expression of ABC transporters in human ovarian carcinoma cells, direct inhibitory activity toward drug efflux pumps was assessed with rhodamine 123 (Rh123; 6-amino-9-(2- methoxycarbonylphenyl) xanthen-3-ylidene]azanium chloride) Cells were initially plated at 2 × 105cells/cm2in 24-well plates and allowed to reach 80 % confluence To assess the ability of cytochalasins to potentiate Rh123

presence and in the absence of cytochalasins or the known P-gp inhibitor verapamil for varying lengths of time At each time point, cells were collected, washed, resuspended

in ice-cold phosphate-buffered saline and kept on ice before fluorescence intensity was measured with flow cytometry Cells were also assessed for their ability to efflux accumu-lated Rh123 in the presence of cytochalasins or verapamil

30 min and then washing the cells twice with ice-cold PBS before being resuspended in fresh Rh123-free medium with and without agents Cells were collected at various time points and were then washed and resuspended in ice-cold PBS before being analyzed by flow cytometry

Determining the extent of drug synergy between cytochalasins, doxorubicin, and paclitaxel

To assess whether cytochalasin B or DiHCB synergizes with doxorubicin or paclitaxel against SK human ovarian carcinomas in vitro, cells were treated alone, or in

both the methylene blue and XTT assays In addition, the Chou-Talalay method for assessing drug synergism was implemented to determine the combination index (CI), dose reduction index (DRI), and fraction affected (Fa) As indicated in [27], synergism was assessed with the following values: CI < 1 (synergy) CI = 1 (additive)

CI > 1 (antagonism) In addition, DRI > 1 is representa-tive of favorable dose reduction, while DRI < 1 is repre-sentative of unfavorable dose reduction [27]

Results

Comparison of cytochalasin congeners and other antineoplastic agents against SK human ovarian carcinoma cell lines

There were notable differences in cytotoxicity between cytochalasin congeners and other antineoplastic agents against the human ovarian carcinoma cell lines Table 2

for nine cytochalasin congeners and for doxorubicin, paclitaxel, and vinblastine While doxorubicin, paclitaxel,

against the parent SKOV3 cell line after a 96 h expos-ure indicative of relatively high efficacy, (11 nM, 2.8

nM, and 1.9 nM, respectively), these agents had

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resistant SKVCR0.015 and SKVCR0.1 lines (125 nM and

125 nM for doxorubicin, 8 nM and 4 nM for paclitaxel,

and 10 nM and 20 nM for vinblastine, respectively),

indica-tive of drug resistance The SKVLB1 cell line showed even

higher resistance to these three agents exhibiting much

respectively; Table 2) The profound differences in

cytotox-icities of these agents against the drug sensitive parental

SKOV3 line compared to the multidrug resistant SKVLB1

line produced very high resistance indices (RI values)

These RI values ranged from 264 for doxorubicin to 1,400

and 1,600 for paclitaxel and vinblastine for SKVLB1 in

comparison with SKOV3

By contrast, cytochalasins did not show this marked

in-crease in resistance against the multidrug resistant SKVLB1

line (Table 2) In fact, cytochalasin A produced a lower IC90

value against SKVLB1 (750 nM) than against SKOV3

(1,000 nM) Interestingly, the most cytotoxic congeners

SKOV3 (cytochalasins C, D, E, and H) had higher RIs

against SKVLB1 than did cytochalasins A, B, J, DiHCB, or

initial cytotoxicity against SKOV3) Nevertheless, the

congener with the highest RI against SKVLB1, cytochalasin

C (RI = 100 against SKVLB1), still had a considerably lower

RI than the clinically approved chemotherapeutic agents (doxorubicin RI = 264, paclitaxel RI = 1,400, and vinblastine

RI = 1,600) The differences in cytotoxicity expressed as

IC90values along with the respective RI values as shown in Table 2 are further highlighted in Fig 2, which uses a loga-rithmic scale to compare the cytotoxicities of agents against SKOV3 and SKVLB1

Effects of a calcium ion channel blocker on cytochalasin-mediated cytotoxicity

As shown in Table 3, the calcium ion channel blocker verapamil increased the drug sensitivity of parental SKOV3

to cytochalasins A, B, and DiHCB by 1.2 to 2-fold Sensitiv-ity to cytochalasins C and D was not enhanced With respect to the highly drug-resistant SKVLB1 line, verapamil did not notably increase cytochalasin A cytotoxicity This presumably reflects the fact that cytochalasin A has slightly enhanced cytotoxicity for SKVLB1 than it does for SKOV3 Sensitivity of SKVLB1 to cytochalasin B or DiHCB was increased by 1.5 fold Very strikingly, the sensitiv-ity of SKVLB1 to cytochalasins C and D was markedly increased by 32- and 64-fold respectively The SK lines with intermediate resistance to SKVLB1 (SKVCR0.015 and SKVCR0.1) showed a 1.5 to 2-fold increase in sensitivity to cytochalasins A, B, and DiHCB when

Table 1 Primer sequences used for reverse transcription polymerase chain reaction to quantify RNA expression of ATP binding cassette transporters in SK human ovarian carcinoma cell lines

Table 2 Effects of clinically approved natural product antineoplastic agents and of cytochalasin congeners on drug-sensitive and multidrug-resistant human ovarian carcinoma lines

ND not determined, RI resistance index compared to parental SKOV3 line

a

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Fig 2 Comparison of clinically approved chemotherapeutic agents and cytochalasin congeners against SKOV3 drug sensitive and SKVLB1 multidrug resistant human ovarian carcinomas Abbreviations used are as follows: ADR (Adriamycin; doxorubicin), Tax (paclitaxel), VBL (vinblastine),

CA (cytochalasin A), CB (cytochalasin B), DiHCB (21,22-dihydrocytochalasin B), CC (cytochalasin C), CD (cytochalasin D), CE (cytochalasin E), CH (cytochalasin H), and CJ (cytochalasin J) The concentration of each agent in nM needed to produce an IC 90 value at 96 h for either cell line is represented on a logarithmic scale The resistance index (RI) of each compound against SKVLB1 is indicated in bold underneath the abbreviations

Table 3 Effects of verapamil on the sensitivity of human ovarian carcinoma cell lines to cytochalasin congeners

Cytochalasin A

-Cytochalasin B

21, 22-Dihydrocytochalasin B

Cytochalasin C

Cytochalasin D

ND not determined, FS fold sensitization

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administered in combination with 15 μM verapamil, and

cytochalasin D had a similar increase in sensitivity with

sensitivity of SKVCR0.1 to cytochalasin C by 2-fold, but did

not affect cytochalasin C with respect to SKVCR0.015 The

carcin-oma sensitivity to cytochalasins B, C, D and DiHCB are

fur-ther highlighted in Fig 3a Verapamil enhanced the

cytotoxicities of cytochalasin B and DiHCB in all four cell

lines tested (black and grey bars), and it enhanced the

cyto-toxicities of cytochalasins C and D against SKVCR0.1 by

1.5 to 2-fold (red and blue bars) The dramatic increases in

cytotoxicities of 32- to 64-fold noted above for

cytochala-sins C and D against the highly drug resistant SKVLB1 line

clearly apparent in Fig 3a

ver-apamil in a 96 h exposure is exhibited at multiple concen-trations of cytochalasin A against SKVCR0.015 (Fig 3b),

as well as with the less potent cytochalasin B against the same cell line (Fig 3c) After continuous exposure for

potential increase in cytotoxicity facilitated by verapamil is further highlighted in dose response growth curves of SKVCR0.015 cells after being treated alone with

a

Cytochalasins were administered alone or

in combination with 30 µM verapamil for 96 hours of continuous exposure.

Numbers in black refer to fold sensitization elicited by the addition of 30 µM verapamil

SKVCR0.015 human ovarian carcinoma with or without 30 µM verapamil after

continuous exposure for 96 hours.

SKVCR0.015 human ovarian carcinoma with or without 30 µM verapamil after

continuous exposure for 96 hours.

2.5 fold increase in sensitivity at 0.5 µM

2.8 fold increase in sensitivity at 0.25 µM.

Fig 3 Effects of verapamil and cytochalasins on SK human ovarian carcinoma cell lines a Effects of verapamil on potentiating SK human ovarian carcinoma sensitivity to cytochalasins B, C, D, and 21,22-dihydrocytochalasin B Cell lines are arranged in order of increasing drug resistance from left to right The IC 90 concentrations are given in μM Numbers in black refer to fold sensitization elicited by the addition of 30 μM verapamil.

b Effects of cytochalasin A-alone or in combination with 30 μM verapamil against SKVCR0.015 cells The values are taken as a percentage of

30 μM verapamil-treated cells c Effects of cytochalasin B-alone or in combination with 30 μM verapamil against SKVCR0.015 cells The values are taken as a percentage of 30 μM verapamil-treated cells d Dose response of cytochalasin A-alone or in combination with 30 μM verapamil on the growth of SKVCR0.015 cells e Dose response of cytochalasin B-alone or in combination with 30 μM verapamil on the growth of SKVCR0.015 cells For panels d and e, agents were administered for either 48 or 96 h, as indicated in the graphs

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48 or 96 h While the addition of verapamil does not

con-siderably increase the percent growth inhibition at most

time points for cytochalasin A (Fig 3d), the calcium ion

channel blocker does potentiate cytochalasin B mediated

growth inhibition, particularly at lower concentrations

(Fig 3e)

Effects of cytochalasins and verapamil on the F/G-actin

ratio found in SK human ovarian carcinoma cells

As expected, cytochalasins demonstrated varying levels of

microfilament inhibition against the parental SKOV3 cells,

with the more potent agents potentiating lower F/G-actin

ratios (Fig 4) In agreement with their IC90 values against

SKOV3, cytochalasin D elicited the lowest F/G actin ratio

after 24 h (8.2), while DiHCBγ-L elicited the highest (20.9)

Interestingly, it appeared that 30μM verapamil had a small,

but notable effect on the F/G-actin ratio of SKOV3 cells

The efficacy of various cytochalasin congeners to inhibit

actin polymerization was notably different in multidrug

resistant SKVLB1 Although the cell line had a smaller, but

notable baseline F/G-actin ratio than its parental

counter-part (27.5 to 31), SKVLB1 was less sensitive to cytochalasin

D inhibition (15.9), but much more sensitive to cytochalasin

was indicated by the four day IC90concentrations The F/

G-actin ratio potentiated by cytochalasin B/verapamil was

lower than cytochalasin B-alone for both SKOV3 (13.4 to

14.3) and SKVLB1 (11.9 to 13.5) The notable decrease in

the F/G actin ratio elicited by the concomitant

administra-tion of cytochalasin B/verapamil follows the same pattern

observed in the cytotoxicity assays of Fig 3, suggesting

verapamil may have a slight, but notable influence on

cyto-chalasin B-mediated cytotoxicity

Assessment of ATP binding cassette transporter overexpression in SK human ovarian carcinomas and the inhibitory effects of cytochalasins and verapamil RT-PCR quantification of ABC transporters revealed that P-gp was substantially overexpressed in the drug resistant derivatives of SKOV3, with expression mirroring the level

of drug resistance associated with each cell line (Fig 5a) The overexpression of P-gp in SKVLB1 in comparison to parental SKOV3 is dramatic as Fig 5a required the use of a logarithmic scale to quantify all expression levels This pat-tern was also observed with MRP2, albeit at lower expres-sion levels, while MRP1 increased only minimally between the four cell lines RT-PCR also revealed that neither

influenced RNA expression, with a slight, but noticeable decrease in P-gp levels against all four neoplastic cell lines Nevertheless, cytochalasins A and B appeared to have notable inhibitory activity against ABC transporters, as assessed by Rh123 accumulation and efflux analysis

cytocha-lasin A or B readily accumulated Rh123, becoming satu-rated by the dye at 60 min (Fig 5b) This activity was also

C, which had only a slight influence on accumulation levels All treatment groups for SKOV3 became saturated

by Rh123, indicative of its low expression of P-gp and other efflux pumps The activity of cytochalasins A and B,

as well as verapamil against ABC transporter-mediated ef-flux of Rh123 was confirmed by experiments in which cells were incubated with the dye prior to being placed in

cytochala-sin C treated SKVLB1 cells effluxed Rh123 at a consistent

Fig 4 Effects of cytochalasin congeners on the F/G-actin ratio of SKOV3 and SKVLB1 human ovarian carcinomas Abbreviations are the same as those used in Fig 2, except for the addition of Ve (verapamil) All cytochalasins were administered at their IC 90 value of 96 h continual exposure, and Ve was administered at 30 μM The F/G-actin ratio of both SKOV3 and SKVLB1 cells was assessed 24 h post-administration Bars represent standard error of the mean (SEM) for each treatment group

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rate with untreated cells reaching 12.4 % content of the

original Rh123 incubation and cytochalasin C treated cells

A or B retained much higher percentages of accumulation

(62.4 % and 53.1 %, respectively), but were less effective

Efficacy of cytochalasin B in increasing drug sensitivity

Cytochalasin B appeared to increase the drug sensitivity of

SKVLB1 cells to clinically approved antineoplastic agents

known to have reduced cytotoxicity against this multidrug

resistant cell line (Table 4) The IC values of doxorubicin

against SKVLB1 cells at 13.5 h and at 33 h of exposure and for paclitaxel at 13.5 h dropped by 2 to 4-fold using

It should be noted that much higher concentrations of

values against SKVLB1 than in earlier determinations because the earlier values were measured at 96 h of expos-ure, while the combination of cytochalasin B with doxo-rubicin or paclitaxel were measured at 13.5 and 33 h

Fig 5 Effects of cytochalasin congeners and verapamil on RNA expression of ATP binding cassette proteins and the efflux of rhodamine 123 in

SK human ovarian carcinoma cell lines a Relative RNA expression of ABCB1 (P-gp), ABCC1 (MRP1), and ABCC2 (MRP2) in SK human ovarian carcinoma cell lines prior to and after treatment with cytochlalasins as assessed by RT-PCR Primer sequences used in the reaction are shown in Table 1 b Cells were treated with the indicated agents, and then exposed to Rh123 c Cells were incubated with Rh123, and then placed in fresh medium The concentrations of each agent used are indicated in the individual panels Bars represent SEM for each treatment group

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Assessment of drug synergy between cytochalasins and clinically approved agents

Both cytochalasin B and DiHCB appeared to synergize with doxorubicin and paclitaxel in SKOV3 and SKVLB1 cells

isobolo-grams (Fig 6) The synergy indicated by these values was also confirmed with Chou-Talalay CI values (Table 5) In addition, DRI values for both the cytochalasins and cur-rently approved agents were indicative of favorable dose reductions, although this would be expected from the isobolograms Interestingly, in both measurements of syn-ergy, it appeared that cytochalasin B and DiHCB synergized with the clinically approved agents more strongly against SKVLB1 than against drug sensitive SKOV3 This syner-gism was noted at other inhibitory concentrations, as indi-cated in Fig 7 Although the individual values may vary, the lines of the Fa-CI plot for SKVLB1 appear to be noticeably

Table 4 Sensitivity to clinically approved antineoplastic agents

potentiated by cytochalasin B against multidrug resistant

SKVLB1 human ovarian carcinoma

Doxorubicin

Paclitaxel

FS fold sensitization

Fig 6 IC 50 isobolograms for cytochalasin B, 21, 22-dihydrocytochalasin B, doxorubicin, and paclitaxel against SKOV3 and SKVLB1 human ovarian carcinoma a CB and ADR b CB and Tax c DiHCB and ADR d DiHCB and Tax IC 50 values were determined after a 48 h continuous exposure

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